Cryo EM structure of a stable LGL/aPKC Iota/Par-6 complex. Determined by electron microscopy at 3.68 Å resolution. Released 20 Nov 2024.
Explore 8R3Y in 3D Show helices and sheets RCSB PDB PDBe
8R3Y contains 47 α-helices and 89 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 251-253 | 3 | |
| β-strand | 255-262 | 8 | 1 |
| β-strand | 266-272 | 7 | 1 |
| β-strand | 279-286 | 8 | 1 |
| α-helix | 293-308 | 16 | |
| β-strand | 318-322 | 5 | 1 |
| β-strand | 327-332 | 6 | 1 |
| α-helix | 333-335 | 3 | |
| β-strand | 339 | 1 | 2 |
| α-helix | 340-347 | 8 | |
| α-helix | 352-372 | 21 | |
| β-strand | 375 | 1 | 3 |
| β-strand | 384-386 | 3 | 2 |
| β-strand | 392-394 | 3 | 2 |
| β-strand | 401 | 1 | 3 |
| α-helix | 404-405 | 2 | |
| β-strand | 410 | 1 | 4 |
| α-helix | 422-426 | 5 | |
| β-strand | 430 | 1 | 4 |
| α-helix | 433-448 | 16 | |
| α-helix | 456 | 1 | |
| α-helix | 459-460 | 2 | |
| β-strand | 466 | 1 | 5 |
| α-helix | 467-476 | 10 | |
| β-strand | 481-482 | 2 | 6 |
| α-helix | 487-497 | 11 | |
| α-helix | 512-518 | 7 | |
| α-helix | 520-523 | 4 | |
| α-helix | 527-531 | 5 | |
| α-helix | 536-537 | 2 | |
| α-helix | 549-551 | 3 | |
| α-helix | 554-557 | 4 | |
| α-helix | 570-573 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 18-21 | 4 | |
| β-strand | 23-31 | 9 | 7 |
| α-helix | 34 | 1 | |
| β-strand | 37-43 | 7 | 8 |
| β-strand | 48-53 | 6 | 8 |
| β-strand | 57-60 | 4 | 8 |
| β-strand | 68-71 | 4 | 8 |
| β-strand | 78-83 | 6 | 9 |
| β-strand | 89-94 | 6 | 9 |
| β-strand | 99-105 | 7 | 9 |
| β-strand | 110 | 1 | 10 |
| β-strand | 112-119 | 8 | 9 |
| β-strand | 141-144 | 4 | 11 |
| β-strand | 151-154 | 4 | 11 |
| β-strand | 160-163 | 4 | 11 |
| β-strand | 170-176 | 7 | 11 |
| α-helix | 178-183 | 6 | |
| β-strand | 198-202 | 5 | 12 |
| β-strand | 210-215 | 6 | 12 |
| β-strand | 219-224 | 6 | 12 |
| β-strand | 229-234 | 6 | 12 |
| α-helix | 239 | 1 | |
| β-strand | 240-243 | 4 | 13 |
| β-strand | 251-256 | 6 | 13 |
| β-strand | 261-265 | 5 | 13 |
| β-strand | 280 | 1 | 13 |
| β-strand | 291-296 | 6 | 14 |
| β-strand | 306-310 | 5 | 14 |
| α-helix | 314-317 | 4 | |
| β-strand | 321-327 | 7 | 14 |
| β-strand | 330-336 | 7 | 14 |
| β-strand | 340-345 | 6 | 15 |
| β-strand | 360-365 | 6 | 15 |
| β-strand | 369-373 | 5 | 15 |
| β-strand | 381 | 1 | 15 |
| α-helix | 390-392 | 3 | |
| β-strand | 395-401 | 7 | 16 |
| α-helix | 406-419 | 14 | |
| β-strand | 436-437 | 2 | 10 |
| α-helix | 439-442 | 4 | |
| β-strand | 447-452 | 6 | 16 |
| β-strand | 456-461 | 6 | 16 |
| β-strand | 469-474 | 6 | 16 |
| α-helix | 476-478 | 3 | |
| β-strand | 479 | 1 | 17 |
| α-helix | 480-481 | 2 | |
| β-strand | 500-503 | 4 | 14 |
| β-strand | 509-510 | 2 | 6 |
| β-strand | 517-523 | 7 | 18 |
| α-helix | 524-526 | 3 | |
| β-strand | 528-533 | 6 | 18 |
| β-strand | 537-544 | 8 | 18 |
| β-strand | 548-550 | 3 | 19 |
| α-helix | 551-552 | 2 | |
| β-strand | 553-557 | 5 | 18 |
| α-helix | 572-575 | 4 | |
| β-strand | 576 | 1 | 17 |
| α-helix | 577-578 | 2 | |
| β-strand | 581-583 | 3 | 19 |
| β-strand | 586-595 | 10 | 18 |
| β-strand | 603-607 | 5 | 20 |
| β-strand | 612-616 | 5 | 20 |
| β-strand | 620-625 | 6 | 20 |
| β-strand | 631-636 | 6 | 20 |
| α-helix | 656 | 1 | |
| β-strand | 657 | 1 | 5 |
| α-helix | 658-659 | 2 | |
| β-strand | 707-709 | 3 | 21 |
| β-strand | 723-731 | 9 | 22 |
| β-strand | 740-747 | 8 | 22 |
| β-strand | 751-758 | 8 | 22 |
| β-strand | 775-783 | 9 | 22 |
| α-helix | 788-789 | 2 | |
| β-strand | 790-796 | 7 | 23 |
| α-helix | 801 | 1 | |
| β-strand | 802 | 1 | 23 |
| α-helix | 803-805 | 3 | |
| α-helix | 808-810 | 3 | |
| α-helix | 816-818 | 3 | |
| α-helix | 822-823 | 2 | |
| β-strand | 824-829 | 6 | 23 |
| β-strand | 832-837 | 6 | 23 |
| β-strand | 840-848 | 9 | 23 |
| α-helix | 849-852 | 4 | |
| β-strand | 857-866 | 10 | 24 |
| β-strand | 874-882 | 9 | 24 |
| β-strand | 887-891 | 5 | 24 |
| β-strand | 896-901 | 6 | 24 |
| α-helix | 909-912 | 4 | |
| β-strand | 916-918 | 3 | 7 |
| β-strand | 922-928 | 7 | 7 |
| β-strand | 931-938 | 8 | 7 |
| β-strand | 947-948 | 2 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 156-160 | 5 | 21 |
| α-helix | 167-169 | 3 | |
| β-strand | 172-178 | 7 | 21 |
| β-strand | 189-194 | 6 | 21 |
| α-helix | 202-205 | 4 | |
| α-helix | 213 | 1 | |
| β-strand | 214-218 | 5 | 21 |
| β-strand | 221-222 | 2 | 21 |
| α-helix | 228-236 | 9 | |
| β-strand | 242-246 | 5 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein kinase C iota type | I | protein | 338 | Homo sapiens | P41743 (AlphaFold model) |
| Lethal(2) giant larvae protein homolog 1 | L | protein | 937 | Homo sapiens | Q15334 (AlphaFold model) |
| Partitioning defective 6 homolog alpha | P | protein | 99 | Homo sapiens | R4GMM2 (AlphaFold model) |
>8R3Y_1 Protein kinase C iota type (chains I) SLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFE QASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALN YLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRG EDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSV KAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEF GLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYI
>8R3Y_2 Lethal(2) giant larvae protein homolog 1 (chains L) REKLKQELFAFNKTVEHGFPNQPSALAFDPELRIMAIGTRSGAVKIYGAPGVEFTGLHRD AATVTQMHFLTGQGRLLSLLDDSSLHLWEIVHHNGCAHLEEALSFQLPSRPGFDGASAPL SLTRVTVVLLVAAGDIAALGTEGSSVFFLDVTTLTLLEGQTLAPGEVLRSVPDDYRCGKA LGPVESLQGHLRDPTKILIGYSRGLLVIWNQASQCVDHIFLGNQQLESLCWGRDSSTVVS SHSDGSYAVWSVDAGSFPTLQPTVATTPYGPFPCKAINKILWRNCESGGHFIIFSGGMPR ASYGDRHCVSVLRAETLVTLDFTSRIIDFFTVHSTRPEDEFDDPQALAVLLEEELVVLDL QTPGWPAVPAPYLAPLHSSAITCSAHVASVPAKLWARIVSAGEQQSPQPVSSALSWPITG GRNLAQEPSQRGLLLTGHEDGTVRFWDASGVALRPLYKLSTAGLFQTDCEHADSLAQAAE DDWPPFRKVGCFDPYSDDPRLGVQKVALCKYTAQMVVAGTAGQVLVLELSDVPVEQAVSV AIIDLLQDREGFTWKGHERLSPRTGPLPWPAGFQPRVLVQCLPPAAVTAVTLHTEWSLVA FGTSHGFGLFDYQRKSPVLARCTLHPNDSLAMEGPLSRVKSLKKSLRQSFRRIRKSRVSG KKRAANASSKLQEANAQLAEQACPHDVEMTPVQRRIEPRSADDSLSGVVRCLYFADTFLR DGAHHGPTMWAGTNSGSVFAYALEVPAAAVGGEKRPEQAVEAVLGKEVQLMHRAPVVAIA VLDGRGRPLPEPYEASRDLAQAPDMQGGHAVLIASEEQFKVFTLPKVSAKTKFKLTAHEG CRVRKVALATFASVACEDYAETCLACLTNLGDVHVFSVPGLRPQVHYSCIRKEDISGIAS CVFTRHGQGFYLISPSEFERFSLSARNITEPLCSLDI
>8R3Y_3 Partitioning defective 6 homolog alpha (chains P) THRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSD EILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Capture, mutual inhibition and release mechanism for aPKC-Par6 and its multisite polarity substrate Lgl. Earl, C.P., Cobbaut, M., Barros-Carvalho, A. et al. Nat Struct Mol Biol (2025) 32:729-739. DOI 10.1038/s41594-024-01425-0 · PubMed
Other PDB entries of the same protein (UniProt P41743 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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